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Introduction of organophosphate compounds, the effectiveness of

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Introduction

The pesticides have facilitated the development and
also expansion of agriculture in world wide. Organophosphate belong to a class
of highly toxic neurotoxins that are commonly used as pesticides and chemical
warfare agent (Surekha Rani et al. 2008).
The continuous use of organophosphate in intensive quantity throughout the
world and their potential neurotoxicity to humans has wind to the development
of various efficient and safety scheme of bioremediation to plenty with their
wide dispersal in the ecosystem (Cho et al. 2002). Enzymatic degradation by
organophosphorus hydrolase (OPH) has received considerable attention. This
attention provides the possibility of both eco friendly and in situ
detoxification (Catherine et al. 2002). The focussing of this study is
organophosphorus hydrolase (OPH, E.C. 8.1.3.1), which catalyzes the hydrolysis
of many organophosphorus compounds and highly reduces the toxicity of organophosphate
pesticide and it can completely mineralize the organophosphate compounds.

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The OPH enzyme was coded by opd gene, were found
in two soil microorganisms namely Pseudomonas diminuta MG and Flavobacterium
sp. (Sethunathan et al. 1998). Although
OPH hydrolyzes a wide range of organophosphate compounds, the effectiveness of
hydrolysis varies dramatically for differnt compounds. Widely used organophosphorus
pesticides like methyl parathion, chlorpyrifos, and diazinon are hydrolyzed slowly
than 30 to 1,000 times is the preferred substrate, paraoxon (Cho et al. 2002).
This reduction in catalytic rate is due to the unfavorable interaction of these
substrates with the active sites involved in catalysis and structural functions
(Zheng et al. 2013).

A number of enzyme are capable of hydrolysing a
number of organophosphate triesters into less or non-toxic compounds. These
enzymes are possible bioremediators because of their ability to decontaminate
OP-containing environment like waters and soils (Zheng et al. 2013). The most
thoroughly characterized phosphotriesterases were isolated from Flavobacterium
sp. ATCC 27551, Pseudomonas diminuta (OPH) and Agrobacterium
radiobacter (OpdA) (Fernanda et al. 2010).
These enzymes belong to the binuclear metallohydrolase family and share
high sequence and structural homology. Phosphotriesterases are highly
promiscuous enzymes, hydrolysing a large range of substrates. The phosphotriester
hydrolysis by OPH had been studied extensively (Castro et al. 2016). In a proposed reaction scheme, based on largely
crystal structures with bound inhibitors, the phosphoryl oxygen of the
substrate binds to the ?-metal ion (Janet et al.2005; Laothanachareo et al. 2008).

In the present research focuses on the interaction
and degradation of chlorpyrifos by OPH enzyme, as this is responsible for
detoxification. The molecular docking study was conducted under FlexX docking
software package. 

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